EFFECTS OF BICARBONATE ON GROWTH OF PASTEURELLA PESTIS. II. CARBON DIOXIDE FIXATION INTO OXALACETATE BY CELL-FREE EXTRACTS
ARMY BIOLOGICAL LABS FREDERICK MD
Pagination or Media Count:
Enzyme preparations from Pasteurella pestis will carboxylate phosphoenolyruvate to form oxalacetate by two distinct reactions. The reactions are similar to those catalyzed by the enzymes phosphoenolpyruvic carboxylase and phosphoenolpyruvate carboxykinase. No significant differences in enzyme characteristics or enzyme content were found when virulent cells were compared with avirulent under the conditions of our experiments. The carboxykinase of P. pestis differs from that of animal origin, as it is dependent upon adenine derivatives rather than inosine or guanosine nucleotides. The latter two nucleotides can act indirectly by way of adenosine nucleotides, as nucleoside diphosphokinase and myokinase are present in the extract.